Evidence map›Paper›PMID 27529623›Full record

ArticlePloS one2016

The Lack of the Essential LptC Protein in the Trans-Envelope Lipopolysaccharide Transport Machine Is Circumvented by Suppressor Mutations in LptF, an Inner Membrane Component of the Escherichia coli Transporter.

Mattia Benedet, Federica A Falchi, Simone Puccio, Cristiano Di Benedetto, Clelia Peano, Alessandra Polissi, Gianni Dehò

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.8field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. ABC Transporters in Bacterial Nanomachineries.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Analyzing the Function of Essential Genes by Plasmid Shuffling.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Characterization of and lipopolysaccharide binding to the E. coli LptC protein dimer.Protein science : a publication of the Protein Society · 2018
    Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Mattia BenedetDipartimento di Bioscienze, Università degli Studi di Milano, Milan, Italy.
Federica A FalchiDipartimento di Bioscienze, Università degli Studi di Milano, Milan, Italy.
Simone PuccioScuola di Dottorato in Medicina Molecolare e Traslazionale, Università degli Studi di Milano, Segrate, Italy.
Cristiano Di BenedettoDipartimento di Bioscienze, Università degli Studi di Milano, Milan, Italy.
Clelia PeanoIstituto di Tecnologie Biomediche, Consiglio Nazionale delle Ricerche, Milan, Italy.
Alessandra PolissiDipartimento di Biotecnologie e Bioscienze, Università degli Studi di Milano-Bicocca, Milan, Italy.
Gianni DehòDipartimento di Bioscienze, Università degli Studi di Milano, Milan, Italy.ORCID http://orcid.org/0000-0001-5492-7766
University of Milan · ITIstituto per le Tecnologie Didattiche · ITUniversity of Milano-Bicocca · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The lipopolysaccharide (LPS) transport (Lpt) system is responsible for transferring LPS from the periplasmic surface of the inner membrane (IM) to the outer leaflet of the outer membrane (OM), where it plays a crucial role in OM selective permeability. In E. coli seven essential proteins are assembled in an Lpt trans-envelope complex, which is conserved in γ-Proteobacteria. LptBFG constitute the IM ABC transporter, LptDE form the OM translocon for final LPS delivery, whereas LptC, an IM-anchored protein with a periplasmic domain, interacts with the IM ABC transporter, the periplasmic protein LptA, and LPS. Although essential, LptC can tolerate several mutations and its role in LPS transport is unclear. To get insights into the functional role of LptC in the Lpt machine we searched for viable mutants lacking LptC by applying a strong double selection for lptC deletion mutants. Genome sequencing of viable ΔlptC mutants revealed single amino acid substitutions at a unique position in the predicted large periplasmic domain of the IM component LptF (LptFSupC). In complementation tests, lptFSupC mutants suppress lethality of both ΔlptC and lptC conditional expression mutants. Our data show that mutations in a specific residue of the predicted LptF periplasmic domain can compensate the lack of the essential protein LptC, implicate such LptF domain in the formation of the periplasmic bridge between the IM and OM complexes, and suggest that LptC may have evolved to improve the performance of an ancestral six-component Lpt machine.

Indexed as

Suppression, GeneticAmino Acid SubstitutionATP-Binding Cassette TransportersBiological TransportCell MembraneEscherichia coliEscherichia coli ProteinsLipopolysaccharidesMembrane ProteinsPhenotypeATP-Binding Cassette TransportersEscherichia coli ProteinsLipopolysaccharidesLptC protein, E coliLptF protein, E coliMembrane Proteins

Identifiers

PMID27529623
PMCPMC4986956
OpenAlexW2510634314

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.